scholarly journals Antisense Silencing of the creA Gene inAspergillus nidulans

2000 ◽  
Vol 66 (10) ◽  
pp. 4579-4581 ◽  
Author(s):  
L. Fernando Bautista ◽  
Alexei Aleksenko ◽  
Morten Hentzer ◽  
Anne Santerre-Henriksen ◽  
Jens Nielsen

ABSTRACT Antisense expression of a portion of the gene encoding the major carbon catabolite repressor CREA in Aspergillus nidulans resulted in a substantial increase in the levels of glucose-repressible enzymes, both endogenous and heterologous, in the presence of glucose. The derepression effect was approximately one-half of that achieved in a null creA mutant. Unlike results for that mutant, however, growth parameters and colony morphology in the antisense transformants were not affected.






2010 ◽  
Vol 56 (3) ◽  
pp. 283-296 ◽  
Author(s):  
Li Tao ◽  
Na Gao ◽  
Sanfeng Chen ◽  
Jae-Hyuk Yu


1999 ◽  
Vol 31 (4) ◽  
pp. 1283-1283 ◽  
Author(s):  
Beatrice Cazelle ◽  
Anna Pokorska ◽  
Elisabeth Hull ◽  
Peter M. Green ◽  
Glyn Stanway ◽  
...  


2020 ◽  
Vol 60 (8) ◽  
pp. 691-698
Author(s):  
Anita Király ◽  
Ivett G. Szabó ◽  
Tamás Emri ◽  
Éva Leiter ◽  
István Pócsi






1993 ◽  
Vol 120 (1) ◽  
pp. 153-162 ◽  
Author(s):  
M J O'Connell ◽  
P B Meluh ◽  
M D Rose ◽  
N R Morris

To investigate the relationship between structure and function of kinesin-like proteins, we have identified by polymerase chain reaction (PCR) a new kinesin-like protein in the filamentous fungus Aspergillus nidulans, which we have designated KLPA. DNA sequence analysis showed that the predicted KLPA protein contains a COOH terminal kinesin-like motor domain. Despite the structural similarity of KLPA to the KAR3 and NCD kinesin-like proteins of Saccharomyces cerevisiae and Drosophila melanogaster, which also posses COOH-terminal kinesin-like motor domains, there are no significant sequence similarities between the nonmotor or tail portions of these proteins. Nevertheless, expression studies in S. cerevisiae showed that klpA can complement a null mutation in KAR3, indicating that primary amino acid sequence conservation between the tail domains of kinesin-like proteins is not necessarily required for conserved function. Chromosomal deletion of the klpA gene exerted no observable mutant phenotype, suggesting that in A. nidulans there are likely to be other proteins functionally redundant with KLPA. Interestingly, the temperature sensitive phenotype of a mutation in another gene, bimC, which encodes a kinesin-like protein involved in mitotic spindle function in A. nidulans, was suppressed by deletion of klpA. We hypothesize that the loss of KLPA function redresses unbalanced forces within the spindle caused by mutation in bimC, and that the KLPA and BIMC kinesin-like proteins may play opposing roles in spindle function.



1997 ◽  
Vol 31 (4) ◽  
pp. 348-356 ◽  
Author(s):  
Jacek Topczewski ◽  
Marzena Sienko ◽  
A. Paszewski


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